-Amylase

Alpha-Amylase

Human salivary amylase: calcium ion visible in pale khaki, chloride ion in green. PDB 1SMD[2] Identifiers 3.2.1.1 EC number 9000-90-2 CAS number Databases IntEnz view IntEnz BRENDA entry BRENDA NiceZyme view ExPASy KEGG entry KEGG metabolic pathway MetaCyc profile PRIAM RCSB PDB PDBe PDBsum PDB structures AmiGO / EGO Gene Ontology [show]Search Main article: alpha-Amylase The -amylases (EC 3.2.1.1 ) (CAS# 9014-71-5) (alternative names: 1,4--D-glucan glucanohydrolase; glycogenase) are calcium metalloenzymes, completely unable to function in the absence of calcium. By acting at random locations along the starch chain, -amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin. Because it can act anywhere on the

substrate, -amylase tends to be faster-acting than -amylase. In animals, it is a major digestive enzyme, and its optimum pH is 6.7-7.0.[3] In human physiology, both the salivary and pancreatic amylases are -amylases. They are discussed in much more detail at alpha-Amylase. This form is also found in plants, fungi (ascomycetes and basidiomycetes) and bacteria (Bacillus)

-Amylase

Beta-Amylase

Structure of barley beta-amylase. PDB 2xfr[4] Identifiers 3.2.1.2 EC number 9000-91-3 CAS number Databases IntEnz view IntEnz BRENDA entry BRENDA NiceZyme view ExPASy KEGG entry KEGG metabolic pathway MetaCyc profile PRIAM RCSB PDB PDBe PDBsum PDB structures AmiGO / EGO Gene Ontology [show]Search Another form of amylase, -amylase (EC 3.2.1.2 ) (alternative names: 1,4--D-glucan maltohydrolase; glycogenase; saccharogen amylase) is also synthesized by bacteria, fungi, and plants. Working from the non-reducing end, -amylase catalyzes the hydrolysis of the second -

1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. During the ripening of fruit, -amylase breaks starch into maltose, resulting in the sweet flavor of ripe fruit. Both -amylase and -amylase are present in seeds; -amylase is present in an inactive form prior to germination, whereas -amylase and proteases appear once germination has begun. Cereal grain amylase is key to the production of malt. Many microbes also produce amylase to degrade extracellular starches. Animal tissues do not contain -amylase, although it may be present in microorganisms contained within the digestive tract. The optimum pH for -amylase is 4.0-5.0[5]

-Amylase

Gamma-Amylase. Glucan 1,4-alphaglucosidase

EC number CAS number IntEnz BRENDA ExPASy KEGG MetaCyc PRIAM PDB structures Gene Ontology Identifiers 3.2.1.3 9032-08-0 Databases IntEnz view BRENDA entry NiceZyme view KEGG entry metabolic pathway profile
RCSB PDB PDBe PDBsum AmiGO / EGO

[show]Search -Amylase (EC 3.2.1.3 ) (alternative names: Glucan 1,4--glucosidase; amyloglucosidase; Exo1,4--glucosidase; glucoamylase; lysosomal -glucosidase; 1,4--D-glucan glucohydrolase) will cleave (1-6) glycosidic linkages, as well as the last (1-4)glycosidic linkages at the nonreducing end of amylose and amylopectin, yielding glucose. The -amylase has most acidic optimum pH of all amylases because it is most active around pH 3.